Carina Lobley

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Carina Lobley is a Senior Support Scientist working accross the MX Village. Carina joined Diamond in 2011 after six years working in industry, using structural biology to understand and optimise the binding of drugs to their target protein.

Email: carina.lobley@diamond.ac.uk
Tel: +44 (0) 1235 778722

Key Research Area

Other Specialist Areas

  • Beamline Development

Latest Publications

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  1. Research Expertise
  2. Collaborations
  3. Publications
Research Expertise -

Current Research Interests

Image Current Research Interests

Protein structure determination has proved an increasingly popular method for gaining insight into protein function, and to activating or deactivating protein activity through binding of drugs. Being able to proceed in a timely fashion from protein target identification to a system compatible with structure determination by X-ray crystallography is a key aim, both in academic and industrial settings.

 
My research is currently focused on the construction and implementation of the VMXi beamline. This beamline will operate entirely automatically, collecting X-ray diffraction data from macromolecular crystals in situ (in the tray in which they were grown). My areas of interest in this research are assessing the data quality from each of the two monochromators available (DCM and DMM), provision of software for users to interact with the beamline and methods for serial and time-resolved crystallography at VMXi. 
 
I have been involved in a number of research activities including:
  • high throughput structure determination in collaboration with the Oxford Protein Production Facility
  • protein crystal dehydration using the HC1b in collaboration with Juan Sanchez-Weatherby
  • integration of RADDOSE with data collection software in collaboration with Elspeth Garman
  • python scripting to optimise beam delivery to users
  • ultra high resolution structure determination
 
Alongside my research my current role at Diamond centers on the support of users before, during and after their beamtime with us. In addition, I undertake the user and user support scheduling and assist with the development of the UAS software to facilitate that role. I have a number of additional responsibilities at Diamond, predominantly assisting in the administration of the MX Village. 

 

Collaborations - +

Collaborations

I have collaborated in work with the Oxford Protein Production Facility (OPPF) and collected X-ray data for a number of different requirements.

                                                    

 

Publications - +

Most recent publications (dec. 2016)

My published research from Diamond Light Source is:

  1. Lobley, Carina M.C. et al. A generic protocol for protein crystal dehydration using the HC1b humidity controller. Acta Crystallographica Section D 72, 629-640
    doi:10.1107/S2059798316003065 (2016).
  2. Lukacik, P. et al. High-resolution structures of Lactobacillus salivarius transketolase in the presence and absence of thiamine pyrophActa Crystallographica Section F 71, 1327-1334, doi:10.1107/S2053230X1501657X (2015).
  3. Aller, P. et al. Application of in situ diffraction in high-throughput structure determination platforms. Methods Mol Biol 1261, 233-253, doi:10.1007/978-1-4939-2230-7_13 (2015).
  4. Mazzorana, M., Sanchez-Weatherby, J., Sandy, J., Lobley, C. M. & Sorensen, T. An evaluation of adhesive sample holders for advanced crystallographic experiments. Acta crystallographica. Section D, Biological crystallography 70, 2390-2400,
    doi:10.1107/S1399004714014370 (2014).
  5. Makhyoun, M. A. et al. The Ni (II) Complex of 2-Hydroxy-Pyridine-N-Oxide 2-Isothionate: Synthesis, Characterization, Biological Studies, and X-ray Crystal Structures using (1) Cu Kα Data and (2) Synchrotron Data. Journal of Materials Science and Nanotechnology 1, 1 (2014),
    doi: 10.15744/2348-9812.1.301
  6. Winter, G., Lobley, C. M. C. & Prince, S. M. Decision making in xia2. Acta Crystallographica Section D 69, 1260-1273, doi:10.1107/S0907444913015308 (2013).
  7. Byrne, R. T., Whelan, Fiona, Aller, Pierre, Bird, Louise E., Dowle, Adam, Lobley, Carina M. C., Reddivari, Yamini, Nettleship, Joanne E., Owens, Raymond J., Antson, Alfred A., Waterman, David G., S-Adenosyl-S-carboxymethyl-l-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoA. Acta Crystallographica Section D 69, 1090-1098,
    doi:10.1107/S0907444913004939 (2013).
  8. Lobley, C. M. C. et al. Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118. Acta Crystallographica Section F 68, 1427-1433,
    doi:10.1107/S174430911204273X (2012).

My PhD, under the supervision of Professor Sir Tom Blundell, involved the structural study of enzymes involved in the pantothenate biosynthesis pathway in E.coli. Publications arising from this work are:

  1. Webb, M. E. et al. Threonine 57 is required for the post-translational activation of Escherichia coli aspartate alpha-decarboxylase. Acta crystallographica. Section D, 70, 1166-1172,
    doi:10.1107/S1399004713034275 (2014).
  2. Webb, M. E. et al. Structure of Escherichia coli aspartate alpha-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation. Acta crystallographica. Section F, Structural biology and crystallization communications 68, 414-417,
    doi:10.1107/S1744309112009487 (2012).
  3. Ciulli, A. et al. pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structuraland calorimetric study. Acta crystallographica. Section D, Biological crystallography 63, 171-178,
    doi:10.1107/S0907444906044465 (2007).
  4. Lobley, C. M. et al. The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound. Biochemistry 44, 8930-8939,
    doi:10.1021/bi0502036 (2005).
  5. Schmitzberger, F. et al. Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase. The EMBO journal 22, 6193-6204, doi:10.1093/emboj/cdg575 (2003).
  6. Lobley, C. M. et al. Structural insights into the evolution of the pantothenate-biosynthesis pathway. Biochemical Society transactions 31, 563-571, doi:10.1042/ (2003).